ALBUMIN ADDUCTS IN PLASMA FROM WORKERS EXPOSED TO TOLUENE DIISOCYANATE

Citation
P. Lind et al., ALBUMIN ADDUCTS IN PLASMA FROM WORKERS EXPOSED TO TOLUENE DIISOCYANATE, Analyst, 122(2), 1997, pp. 151-154
Citations number
14
Categorie Soggetti
Chemistry Analytical
Journal title
ISSN journal
00032654
Volume
122
Issue
2
Year of publication
1997
Pages
151 - 154
Database
ISI
SICI code
0003-2654(1997)122:2<151:AAIPFW>2.0.ZU;2-5
Abstract
Desalted plasma from a 2,4- and 2,6-toluene diisocyanate (2,4- and 2,6 -TDI) exposed worker at a factory producing flexible polyurethane foam was separated and fractionated into 200 fractions using ion-exchange chromatography followed by a gel-filtration separation and fractionati on into 59 fractions, The corresponding amines (to the isocyanates), 2 ,4- and 2,6-toluenediamine (2,4- and 2,6-TDA), were determined in each fraction after sulfuric acid hydrolysis as pentafluoropropionic anhyd ride derivatives by capillary gas chromatography and chemical ionisati on mass spectrometry monitoring negative ions, The ion exchange fracti ons containing TDA (81-115) were added together and the solution was s eparated and fractionated on the gel-filtration column, The fractions 81-115 contained 84 and 72% of 2,4- and 2,6-TDA, respectively, as comp ared to the unfractionated plasma, The gel filtration fractions 22-27 contained 107 and 119% of 2,4- and 2,6-TDA, respectively, as compared to the amounts in the ion exchange fractions (81-115), Agarose gel-ele ctrophoresis and electroimmunoassay demonstrated that albumin, 2,4- an d 2,6-TDA co-eluted in both ion-exchange and gel-filtration chromatogr aphy, Quantitative determination of albumin, 2,4- and 2,6-TDA also dem onstrated that these components co-eluted using albumin-immunosorption chromatography. In addition, studies of affinity isolated IgG reveale d that this fraction was devoid of 2,4- and 2,6-TDA, These results ind icate that albumin is the major receptor molecule for 2,4- and 2,6-TDI in blood plasma and that these isocyanates form covalent bondings wit h albumin.